tailieunhanh - The cyclooxygenases NV Chandrasekharan and Daniel L Simmons

Cyclooxygenases (COXs) catalyze the rate-limiting step in the production of prostaglandins, bioactive compounds involved in processes such as fever and sensitivity to pain, and are the target of aspirin-like drugs. COX genes have been cloned from coral, tunicates and vertebrates, and in all the phyla where they are found, there are two genes encoding two COX isoenzymes; it is unclear whether these genes arose from an early single duplication event or from multiple independent duplications in evolution. The. | Protein family review The cyclooxygenases NV Chandrasekharan and Daniel L Simmons Address Department of Chemistry and Biochemistry Brigham Young University Provo UT 84602 USA. Correspondence NV Chandrasekharan. E-mail nchandra@ Published 27 August 2004 Genome Biology 2004 5 241 The electronic version of this article is the complete one and can be found online at http 2004 5 9 24l 2004 BioMed Central Ltd Summary Cyclooxygenases COXs catalyze the rate-limiting step in the production of prostaglandins bioactive compounds involved in processes such as fever and sensitivity to pain and are the target of aspirin-like drugs. COX genes have been cloned from coral tunicates and vertebrates and in all the phyla where they are found there are two genes encoding two COX isoenzymes it is unclear whether these genes arose from an early single duplication event or from multiple independent duplications in evolution. The intron-exon arrangement of COX genes is completely conserved in vertebrates and mostly conserved in all species. Exon boundaries largely define the four functional domains of the encoded protein the amino-terminal hydrophobic signal peptide the dimerization domain the membrane-binding domain and the catalytic domain. The catalytic domain of each enzyme contains distinct peroxidase and cyclooxygenase active sites COXs are classified as members of the myeloperoxidase family. All COXs are homodimers and monotopic membrane proteins inserted into only one leaflet of the membrane and they appear to be targeted to the lumenal membrane of the endoplasmic reticulum where they are N-glycosylated. In mammals the two COX genes encode a constitutive isoenzyme COX-l and an inducible isoenzyme COX-2 both are of significant pharmacological importance. Gene organization and evolutionary history Cyclooxygenases COXs also known as prostaglandin H synthases or prostaglandin endoperoxide synthases . are fatty-acid oxygenases of the .

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